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Structure paper

TitleStructure of a paramyxovirus polymerase complex reveals a unique methyltransferase-CTD conformation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 9, Page 4931-4941, Year 2020
Publish dateMar 3, 2020
AuthorsRyan Abdella / Megha Aggarwal / Takashi Okura / Robert A Lamb / Yuan He /
PubMed AbstractParamyxoviruses are enveloped, nonsegmented, negative-strand RNA viruses that cause a wide spectrum of human and animal diseases. The viral genome, packaged by the nucleoprotein (N), serves as a ...Paramyxoviruses are enveloped, nonsegmented, negative-strand RNA viruses that cause a wide spectrum of human and animal diseases. The viral genome, packaged by the nucleoprotein (N), serves as a template for the polymerase complex, composed of the large protein (L) and the homo-tetrameric phosphoprotein (P). The ∼250-kDa L possesses all enzymatic activities necessary for its function but requires P in vivo. Structural information is available for individual P domains from different paramyxoviruses, but how P interacts with L and how that affects the activity of L is largely unknown due to the lack of high-resolution structures of this complex in this viral family. In this study we determined the structure of the L-P complex from parainfluenza virus 5 (PIV5) at 4.3-Å resolution using cryoelectron microscopy, as well as the oligomerization domain (OD) of P at 1.4-Å resolution using X-ray crystallography. P-OD associates with the RNA-dependent RNA polymerase domain of L and protrudes away from it, while the X domain of one chain of P is bound near the L nucleotide entry site. The methyltransferase (MTase) domain and the C-terminal domain (CTD) of L adopt a unique conformation, positioning the MTase active site immediately above the poly-ribonucleotidyltransferase domain and near the likely exit site for the product RNA 5' end. Our study reveals a potential mechanism that mononegavirus polymerases may employ to switch between transcription and genome replication. This knowledge will assist in the design and development of antivirals against paramyxoviruses.
External linksProc Natl Acad Sci U S A / PubMed:32075920 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.4 - 4.63 Å
Structure data

21095

6v85

EMDB-21095, PDB-6v85:
Parainfluenza virus 5 L-P complex
Method: EM (single particle) / Resolution: 4.38 Å

21096

6v86

EMDB-21096, PDB-6v86:
Parainfluenza virus 5 L-P complex with an alternate conformation of the CD-MTase-CTD module
Method: EM (single particle) / Resolution: 4.63 Å

PDB-6vag:
Crystal structure of the oligomerization domain of phosphoprotein from parainfluenza virus 5
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

Source
  • simian virus 5 (strain w3)
  • parainfluenza virus 5 (strain w3)
KeywordsVIRAL PROTEIN / POLYMERASE / METHYLTRANSFERASE / POLY-RIBONUCLEOTIDYLTRANSFERASE / Paramyxovirus / Phosphoprotein / Oligomerization domain

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